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. Author manuscript; available in PMC: 2012 Oct 11.
Published in final edited form as: Curr Biol. 2011 Sep 22;21(19):1615–1623. doi: 10.1016/j.cub.2011.08.033

Figure 6. Docking sites drive cyclin-specific phosphorylation.

Figure 6

(A) Phosphorylation of a single substrate (Ste51–260) was monitored with and without the addition of the indicated docking sites, in cells expressing different PGAL1-induced cyclins. Docking sites from Ste5, Ste20, and Exo84 preferentially enhance phosphorylation by Cln1/2-Cdc28, whereas an RxL-containing fragment from Fin1 converts the substrate into one that is preferred by Clb5 and Clb2

(B) Schematic comparison of different cyclin-Cdk complexes, with a general model for how cyclin-specific docking interactions can selectively enhance substrate phosphorylation by individual forms of cyclin-Cdk.